Multiple enzyme approach for the characterization of glycan modifications on the C-terminus of the intestinal MUC2mucin.

ABSTRACT: The polymeric mucin MUC2 constitutes the main structural component of the mucus that covers the colon epithelium. The protein's central mucin domain is highly O-glycosylated and binds water to provide lubrication and prevent dehydration, binds bacteria, and separates the bacteria from the epithelial cells. Glycosylation outside the mucin domain is suggested to be important for proper protein folding and protection against intestinal proteases. However, glycosylation of these regions of the MUC2 has not been extensively studied. A purified 250 kDa recombinant protein containing the last 981 amino acids of human MUC2 was produced in CHO-K1 cells. The protein was analyzed before and after PNGase F treatment, followed by in-gel digestion with trypsin, chymotrypsin, subtilisin, or Asp-N. Peptid

SUBMITTER: van der Post S 

PROVIDER: S-EPMC4261943 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature